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Role of Fe2+ in Oxygen Sensing in the Carotid Body

  • S. Lahiri
  • A. Roy
  • J. Li
  • S. M. Baby
  • A. Mokashi
  • C. Di Giulio
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 551)

Abstract

Prolyl hydroxylase is an enzyme which oxidatively modifies the proline residue of hypoxia inducible factor (HIF-lα) in the presence of oxygen in an apparently irreversible reaction. This reaction also requires labile Fe2+, 2-oxogluterate (2-OG) and ascorbic acid. Hypoxia retards this reaction and HIF-1α is accumulated. Similarly, Fe2+ chelation mimics hypoxia-like effect. Thus, the enzyme stands at the gateway between hypoxia and normoxia. The hy-droxylated HIF-1α undergoes proteasomal degradation during normoxia whereas HIF-1α, accumulated during hypoxia, binds with β-subunits to form HIF-1 which is then transcripted to various genes in the nucleus.

Keywords

Iron Chelation Carotid Body Prolyl Hydroxylase Glomus Cell Mitochondrial Inhibitor 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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Copyright information

© Kluwer Academic/Plenum Publishers, New York 2004

Authors and Affiliations

  • S. Lahiri
    • 1
  • A. Roy
    • 1
  • J. Li
    • 1
  • S. M. Baby
    • 1
  • A. Mokashi
    • 1
  • C. Di Giulio
    • 2
  1. 1.Dept. of PhysiologyUniversity of Pennsylvania Medical CenterPhiladelphiaUSA
  2. 2.Dept. of Biomedical SciencesG. d’Annunzio UniversityChietiItaly

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